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Molecular interactions of glycopeptide antibiotics investigated by affinity capillary electrophoresis and bioaffinity electrospray ionization‐mass spectrometry
Author(s) -
Vollmerhaus Pauline J.,
Tempels F. W. Alexander,
Kettenesvan den Bosch J. Jantina,
Heck Albert J. R.
Publication year - 2002
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/1522-2683(200203)23:6<868::aid-elps868>3.0.co;2-#
Subject(s) - capillary electrophoresis , glycopeptide , electrospray ionization , chromatography , mass spectrometry , capillary electrophoresis–mass spectrometry , chemistry , electrospray , electrophoresis , antibiotics , biochemistry
Many analytical approaches are available to evaluate (bio)molecular interactions, all of which have their particular advantages and disadvantages. In recent years, two relatively new techniques have emerged that may be used by the bioanalytical community to evaluate such interactions, namely affinity capillary electrophoresis (ACE) and bioaffinity electrospray ionization‐mass spectrometry (ESI‐MS). In this paper, we describe and evaluate the use of both these techniques for the investigation of the interactions of glycopeptide antibiotics with peptides that mimic the bacterial cell wall binding site. We focus particularly on the effect of the sugar moieties attached to the antibiotic peptide backbone and on the noncovalent dimerization of these glycopeptide antibiotics.